1U5O

Structure of the D23A mutant of the nuclear transport carrier NTF2

Summary for 1U5O

• Entry DOI: 10.2210/pdb1u5o/pdb
• Related: 1OUN 1ar0 1ask
• Descriptor: Nuclear transport factor 2 (2 entities in total)
• Functional Keywords: transport, nuclear transport protein, ntf2 mutant d23a, protein transport
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm (By similarity): P61972
• Total number of polymer chains: 2
• Total formula weight: 28894.83

Authors

Cushman, I.,Bowman, B.R.,Sowa, M.E.,Lichtarge, O.,Quiocho, F.A.,Moore, M.S. (deposition date: 2004-07-28, release date: 2004-12-07, Last modification date: 2024-02-14)

Primary citation

Cushman, I.,Bowman, B.R.,Sowa, M.E.,Lichtarge, O.,Quiocho, F.A.,Moore, M.S.
Computational and biochemical identification of a nuclear pore complex binding site on the nuclear transport carrier NTF2.
J.Mol.Biol., 344:303-310, 2004

PubMed Abstract: Nuclear transport carriers interact with proteins of the nuclear pore complex (NPC) to transport their cargo across the nuclear envelope. One such carrier is nuclear transport factor 2 (NTF2), whose import cargo is the small GTPase Ran. A domain highly homologous to the small NTF2 protein (14kDa) is also found in a number of additional proteins, which together make up the NTF2 domain containing superfamily of proteins. Using structural, computational and biochemical analysis we have identified a functional site that is present throughout this superfamily, and our results indicate that this site functions as an NPC binding site in NTF2. Previously we showed that a D23A mutant of NTF2 exhibits increased affinity for the NPC. The mechanism of this mutation, however, was unknown as this region of NTF2 had not been implicated in binding to NPC proteins. Here we show that the D23A mutation in NTF2 does not result in gross structural changes affecting other known NPC binding sites. Instead, the D23 residue is located in an evolutionarily important region in the NTF2 domain containing superfamily, that in NTF2, is involved in binding to the NPC.

PubMed: 15522285
DOI: 10.1016/j.jmb.2004.09.043

Experimental method

X-RAY DIFFRACTION (2.5 Å)